association constant


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Related to association constant: dissociation constant

association constant

[ə‚sō·sē′ā·shən ¦kän·stənt]
(biochemistry)
A quantitative description of the affinity of a ligand for a protein that binds to it.
References in periodicals archive ?
In addition, the association constant (Kc) [22] and standard free energy changes (IGAdeg) [22] have also been evaluated.
The binding data are listed in Table 1, showing that the receptor binds strongly to S[O.sub.4.sup.2-], with an association constant larger than [10.sup.4] [M.sup.-1] (Table 1).
Scatchards plot used for measurement of specific binding of compounds with BSA at different composition and from which the value of association constant are calculated.
For fast kinetics parameters measurement, affinity interactions between biotin and avidin were characterized by the association rate constant [k.sub.a], the dissociation rate constant [k.sub.d], and the equilibrium association constant [K.sub.eq].
SD RSD (%) ([micro]g/mL) ([micro]g/mL) I 9.10 9.13 0.021 0.23 II 9.10 9.16 0.030 0.33 III 9.10 9.05 0.033 0.37 IV 9.10 9.08 0.026 0.29 V 9.10 9.09 0.022 0.24 VI 9.10 9.00 0.035 0.39 VII 9.10 9.06 0.025 0.28 VIII 9.10 9.07 0.026 0.29 Table 3: Association constant and free energy ([DELTA][G.sup.[omicron]]) obtained from the molar ratio and continuous variation method of ion-associate complexes under investigation.
(II) Association/dissociation of Bb-cC (association constant [k.sub.2]; dissociation constant [l.sub.2]):
where [K.sub.ass] is the association constant on the complex (TS) and is the equilibrium constant of this heterogeneous reaction at the interface feed phase-membrane; [[T].sub.i] is the carrier concentration at the interface membrane-feed phase; and [S]; is the substrate concentration in the source phase at the membrane interface.
To compare quantitatively the binding strength of the Hf[O.sub.2] NPs, the apparent association constants [K.sub.app] of Hf[O.sub.2] NPs with HSA were obtained by monitoring the changes in absorbance at 278nm for HSA.
To determine the association constants [K.sub.a], we assumed that the detected fluorescence quenching is based on formation of a [BSA-L] complex with decreased fluorescence emission.
where [F.sub.0] and F are the fluorescence intensities of HSA in the absence and presence of the quencher (isoimperatorin), respectively, [K.sub.b] is the association constant, and n is the number of binding sites per HSA [25].

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